Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins

Journal of Biological Chemistry

Volumn 280, Issue 35, 2005, Pages 31249-31256

  Sauvage, Eric ^a   Herman, Raphael ^a   Petrella, Stephanie ^a   Duez, Colette ^a   Bouillenne, Fabrice ^a   Frère, Jean Marie ^a   Charlier, Paillette ^a  

^a UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BINDING ENERGY; BIOCHEMISTRY; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GENETIC ENGINEERING; RATE CONSTANTS;

ACTINOMADURA R39 DD-PEPTIDASE; ACYL-ENZYME COMPLEX; HELICES; PENICILLIN- BINDING PROTEIN (PBP);

ENZYMES;

BETA LACTAM ANTIBIOTIC; COBALT; NITROCEFIN; PENICILLIN BINDING PROTEIN; PENICILLIN G; PEPTIDASE; SERINE;

ACTINOMADURA; ACYLATION; ARTICLE; BETA SHEET; BINDING AFFINITY; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE;

ACTINOMYCETALES; BACTERIAL PROTEINS; CEPHALOSPORINS; COBALT; CRYSTALLOGRAPHY, X-RAY; INDICATORS AND REAGENTS; MODELS, MOLECULAR; PENICILLINS; PROTEIN STRUCTURE, TERTIARY; SERINE-TYPE D-ALA-D-ALA CARBOXYPEPTIDASE;

ACTINOMADURA; ACTINOMADURA SP.; ESCHERICHIA COLI;

EID: 24744431864     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M503271200     Document Type: Article

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